Journal
COMPTES RENDUS BIOLOGIES
Volume 328, Issue 8, Pages 701-712Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.crvi.2005.02.007
Keywords
protein function; temperature jump; hydrophobicity; activation barrier
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Proteins can be redesigned to fold downhill on a free energy surface characterized by only a few coordinates, confirming a principal prediction of the 'energy-landscape' model. Nonetheless, natural proteins have small but significant barriers. Spectroscopy and kinetics reveal potential biological causes for activation barriers during protein folding: evolution against protein aggregation and for protein function.
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